ID   A0A319D0N7_9EURO        Unreviewed;       613 AA.
AC   A0A319D0N7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Carbon catabolite repression protein cred {ECO:0000313|EMBL:PYH91056.1};
GN   ORFNames=BO71DRAFT_333078 {ECO:0000313|EMBL:PYH91056.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH91056.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH91056.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH91056.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Interacts with hulA. {ECO:0000256|ARBA:ARBA00038766}.
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DR   EMBL; KZ825958; PYH91056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319D0N7; -.
DR   STRING; 1448320.A0A319D0N7; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   Gene3D; 2.60.40.640; -; 1.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11188:SF175; ARRESTIN-RELATED TRAFFICKING ADAPTER 5; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT   DOMAIN          181..332
FT                   /note="Arrestin C-terminal-like"
FT                   /evidence="ECO:0000259|SMART:SM01017"
FT   REGION          376..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  68204 MW;  4DDCB83C11ECBAE3 CRC64;
     MALSFFGGGG SASYAKYFDI RLDEDYIVFR GGEEEAASAH LSGKLILCLS EPLSIKHIRL
     HLTGISRVCW HLPSSTAGGG RKSWRERVFY EKTWRFRDAG KSKTEVLPAG NYEYPFNIVL
     EGSMPESVEG LSDTYVTYRF KAEIGRKYAK DIIVRRPLRI IRTLEPSALE LAHAMSVENV
     WPNKIEYSIS TPTKAVVFGT CLRVDFKLIP LLKGLRIGQI VSQLIESHDL TLNPEDPDSI
     RNTYKSTRTI LNDEHELDED NGLEIIDEMA EGYQFSRHLE LPKTLTRCLQ DTDTRGIKIR
     HKLKFRVQLL NPDGHVSELR ATLPVSIFIS PSLAIDENNN LVDQTPQSAQ RAVDDLAQQA
     PPLYGEHTFD QLYSQVDPSG YRTPGPGSGG AGTPFGTLSR NLSTENLASM NALTNTDISA
     SALHSRLSSL RANGHNLNHN HNGHFHPGSP PEHEPHPEID PRRLNIPPDY FSVAPTSGSN
     SHSPTSPELS RRPSDEVDHD YIHSGMATPY HPQYAEVETL SRVPSYSTAV RTTVRPCDSD
     LPDYSSVIAE DVVISAPQSP QQAYIRTAGR GGSSYFSAID ALHSRSGLLH PRSTSHDDEE
     ERRLRLVQAR ARV
//